Available hosts

Available applications

Background of PFKFB1 antibody

PFKFB (6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase) is a bifunctional enzyme, having both kinase and phosphatase activities residing on the same enzyme subunit but having distinct active sites. PFKFB regulates the steady-state concentration of fructose-2,6-bisphosphate, a potent activator of a key regulatory enzyme of glycolysis, phosphofructokinase. To date, four PFKFB isozymes (PFKFB 1-4) have been described, which show differences in their tissue distribution and kinetic properties in response to allosteric effectors and hormonal signals. Among the PFKFB's PFKFB3 has the highest kinase:phosphatase ratio, in part because it lacks the characteristic serine phosphorylation site near the N-terminal that down-modulates kinase activity. PFKFB3 was first described in the rapidly growing placenta. The glucolitic rate in placenta is accelerated by anoxia and by maternal diabetes. Cancer cells maintain a high glycolytic rate even in the presence of oxygen, a phenomenon known as the Warburg effect. The glycolytic rate in the placenta, another fast-growing tissue, is accelerated by anoxia and by maternal diabetes.

Formalin-fixed and paraffin-embedded human hepatocarcinoma tissue reacted with PFKFB1 polyclonal antibody ( Cat # PAB4020 ) , which was peroxidase-conjugated to the secondary antibody, followed by DAB staining.This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated.

Formalin-fixed and paraffin-embedded human hepatocarcinoma tissue reacted with PFKFB1 polyclonal antibody ( Cat # PAB4021 ) , which was peroxidase-conjugated to the secondary antibody, followed by DAB staining.This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated.